2F23

Crystal structure of GreA factor homolog 1 (Gfh1) protein of Thermus thermophilus

2F23 の概要

• エントリーDOI: 10.2210/pdb2f23/pdb
• 分子名称: Anti-cleavage anti-greA transcription factor gfh1 (2 entities in total)
• 機能のキーワード: crystal structure anti-grea gfh1 thermus thermophilus, transcription
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34356.94

構造登録者

Kong, X.P.,Kim, S.-S. (登録日: 2005-11-15, 公開日: 2006-05-30, 最終更新日: 2024-02-14)

主引用文献

Laptenko, O.,Kim, S.-S.,Lee, J.,Starodubtseva, M.,Cava, F.,Berenguer, J.,Kong, X.P.,Borukhov, S.
pH-dependent conformational switch activates the inhibitor of transcription elongation.
Embo J., 25:2131-2141, 2006

PubMed Abstract: Gfh1, a transcription factor from Thermus thermophilus, inhibits all catalytic activities of RNA polymerase (RNAP). We characterized the Gfh1 structure, function and possible mechanism of action and regulation. Gfh1 inhibits RNAP by competing with NTPs for coordinating the active site Mg2+ ion. This coordination requires at least two aspartates at the tip of the Gfh1 N-terminal coiled-coil domain (NTD). The overall structure of Gfh1 is similar to that of the Escherichia coli transcript cleavage factor GreA, except for the flipped orientation of the C-terminal domain (CTD). We show that depending on pH, Gfh1-CTD exists in two alternative orientations. At pH above 7, it assumes an inactive 'flipped' orientation seen in the structure, which prevents Gfh1 from binding to RNAP. At lower pH, Gfh1-CTD switches to an active 'Gre-like' orientation, which enables Gfh1 to bind to and inhibit RNAP.

PubMed: 16628221
DOI: 10.1038/sj.emboj.7601094

実験手法

X-RAY DIFFRACTION (1.6 Å)